Phosphorylation of the skeletal muscle AMP-deaminase by protein kinase C.
Protein kinase C catalyzes phosphorylation of the rat skeletal muscle AMP-deaminase in the presence of calcium ions and phosphatidylserine. At the same time, the catalytic subunit of cAMP-dependent protein kinase fails to phosphorylate AMP-deaminase. Ca2+, phosphatidylserine-dependent phosphorylation decreases three-fold (from 0.6 to 0.2 mM) the Km value and does not affect Vmax. Protein kinase C-induced phosphorylation of AMP-deaminase, besides ADP-ribosylation, is suggested to be involved in regulating the AMP-deaminase activity in vivo.
Tovmasian
E K
EK
Institute of Biochemistry, Academy of Sciences of Arm, SSR, Yerevan.
Hairapetian
R L
RL
Bykova
E V
EV
Severin
S E
SE
Haroutunian
A V
AV
D000659:AMP Deaminase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009709:Nucleotide Deaminases / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D011493:Protein Kinase C; D009709:Nucleotide Deaminases; D000659:AMP Deaminase